Results 251 to 260 of about 32,058 (267)
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The phenylalanine ammonia-lyase gene family in Arabidopsis thaliana
Plant Molecular Biology, 1995Phenylpropanoid derivatives are a complex class of secondary metabolites that have many important roles in plants during normal growth and in responses to environmental stress. Phenylalanine ammonialyase (PAL) catalyzes the first step in the biosynthesis of phenylpropanoids, and is usually encoded by a multi-gene family.
Guoqing Li +4 more
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Activity of l-phenylalanine ammonia-lyase in organic solvents
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997L-Phenylalanine ammonia-lyase (EC 4.3.1.5), (PAL) was shown to be active in a monophasic non-aqueous medium for the first time. Ultraviolet absorbance spectra of trans-cinnamic acid were shown to be similar in both water and n-octanol. High catalytic rates were observed only when the enzyme was placed in solvents containing high concentrations of water.
D. Hugh Jones, D. Gareth Rees
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Tissue and method specificities of phenylalanine ammonia-lyase assay
Journal of Plant Physiology, 2012A large number of studies have estimated phenylalanine ammonia-lyase (PAL) activity because it strongly reacts to various stimuli. Activity of this enzyme has been assayed mainly by means of spectrophotometry, but the precision of this method is poorly known.
Bořivoj Klejdus +3 more
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Functional Plant Biology, 1980
In constant light, whole apples (cv. Red Spy) that received alternating 6/25°C treatment accumulated more phenylalanine ammonia-lyase (PAL) and anthocyanin than those receiving constant 25° throughout the course of experiment. The stimulatory effect of low temperature (6°) on the activity of PAL and synthesis of anthocyanin was also observed in the ...
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In constant light, whole apples (cv. Red Spy) that received alternating 6/25°C treatment accumulated more phenylalanine ammonia-lyase (PAL) and anthocyanin than those receiving constant 25° throughout the course of experiment. The stimulatory effect of low temperature (6°) on the activity of PAL and synthesis of anthocyanin was also observed in the ...
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Protection of phenylalanine ammonia-lyase from proteolytic attack
Biochemical and Biophysical Research Communications, 1985Phenylalanine ammonia-lyase contained within permeabilized cells of Rhodosporidium toruloides was protected from proteolytic attack by trypsin, chymotrypsin and duodenal juice. The inactivation by the proteases was biphasic. The enzyme contained within the yeast cells had a similar Km for phenylalanine and Ki for cinnamic acid to the protein in free ...
Michael Tully, Harry J. Gilbert
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Mimicking the Reaction of Phenylalanine Ammonia Lyase by a Synthetic Model
Helvetica Chimica Acta, 2000AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Rettig, Martin +2 more
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Tyrosine and phenylalanine ammonia lyases in Sporobolomyces roseus
1968The enzymes phenylalanine ammonia lyase (PAL) and tyrosine ammonia lyase (TAL) were studied in the yeast Sporobolomyces roseus (Kluyver and van Neil). Cells grown on a glucose-salts medium were ground with alumina, and the cell-free buffer extract was fractionated with ammonium sulfate.
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Recombinant phenylalanine ammonia lyase in phenylketonuria
The Lancet, 2014Francjan J. van Spronsen +1 more
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Archives of Biochemistry and Biophysics, 1981
Abstract A preparation of l -phenylalanine ammonia-lyase (EC 4.1.3.5.) from soybean ( Glycine max L. cv. Kanrich) showed negative cooperativity with respect to l -phenylalanine and competitive inhibition by d -phenylalanine. A two-protomer partially concerted model for inhibition kinetics is described.
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Abstract A preparation of l -phenylalanine ammonia-lyase (EC 4.1.3.5.) from soybean ( Glycine max L. cv. Kanrich) showed negative cooperativity with respect to l -phenylalanine and competitive inhibition by d -phenylalanine. A two-protomer partially concerted model for inhibition kinetics is described.
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